Y105E8A.14 E3 ubiquitin-protein ligase [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: Y105E8A.14
Official Full Name: E3 ubiquitin-protein ligase
Primary source: WormBase:WBGene00013674
Locus tag: CELE_Y105E8A.14
See related: AllianceGenome:WB:WBGene00013674
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Caenorhabditis elegans (strain: Bristol N2)
Lineage: Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary: Predicted to enable poly-ADP-D-ribose binding activity and ubiquitin-protein transferase activity. Predicted to be involved in ubiquitin-dependent protein catabolic process. Predicted to be located in cytosol. Predicted to be active in cytoplasm and nucleus. Is expressed in intestine; marginal cell; pharyngeal muscle cell; and rectal gland cell. Orthologous to human RNF146 (ring finger protein 146). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See Y105E8A.14 in Genome Data Viewer

Location:: chromosome: I

Exon count:: 2

Sequence:: Chromosome: I; NC_003279.8 (14465380..14468214, complement)

Chromosome I - NC_003279.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003279.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Y105E8C.e (e-PCR)
- UniSTS:324538

Y105E8C.f (e-PCR)
- UniSTS:324032

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables poly-ADP-D-ribose binding	IBA Inferred from Biological aspect of Ancestor more info
enables poly-ADP-D-ribose binding	IEA Inferred from Electronic Annotation more info
enables transferase activity	IEA Inferred from Electronic Annotation more info
enables ubiquitin protein ligase activity	IEA Inferred from Electronic Annotation more info
enables ubiquitin-protein transferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables zinc ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in Wnt signaling pathway	IEA Inferred from Electronic Annotation more info
involved_in protein autoubiquitination	IEA Inferred from Electronic Annotation more info
involved_in ubiquitin-dependent protein catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in ubiquitin-dependent protein catabolic process	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	IEA Inferred from Electronic Annotation more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: E3 ubiquitin-protein ligase

NP_740943.2

Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_003279.8 Reference assembly

Range

14465380..14468214 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_170947.6 → NP_740943.2 E3 ubiquitin-protein ligase [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_740943.2

Status: REVIEWED

UniProtKB/TrEMBL

Q8WQB0

Conserved Domains (2) summary

smart00678
Location:130 → 202

WWE; Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis

cd00162
Location:23 → 67

RING; RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc; defined by the 'cross-brace' motif C-X2-C-X(9-39)-C-X(1-3)- H-X(2-3)-(N/C/H)-X2-C-X(4-48)C-X2-C; probably involved in ...